IntAct European Bioinformatics Institute IntAct intact http://www.ebi.ac.uk/ http://www.ebi.ac.uk/intact/query/${ac} EBI-[0-9]+|IA:[0-9]+ INTerAction database (IntAct) provides an open source database and toolkit for the storage, presentation and analysis of molecular interactions. http://www.ebi.ac.uk/intact European Bioinformatics Institute; Wellcome Trust Genome Campus; Hinxton, Cambridge; CB10 1SD; United Kingdom http://www.ebi.ac.uk/intact/ http://www.ebi.ac.uk/ cotman-2000-3 Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. human Homo sapiens Human light microscopy light microscopy immunostaining immunostaining Cotman SL., Halfter W., Cole GJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Paraffin or frozen sections of Alzheimer's disease brains pretreated with formic acid and stained woth polyclonal antisera recognising Abeta (1-40) or human Agrin. Abeta (1-40) peptide sequence confirmed to correspond to human sequence following correspondence with author (GC). gcole@nccu.edu Mol. Cell. Neurosci. (1044-7431) 2000 Only protein-protein interactions imex curation Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Alzheimers - Interactions investigated in the context of Alzheimers disease cotman-2000-2 Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. in vitro In vitro cosedimentation cosedimentation western blot western blot Immuno blot Immuno blot Cotman SL., Halfter W., Cole GJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Paraffin or frozen sections of Alzheimer's disease brains pretreated with formic acid and stained woth polyclonal antisera recognising Abeta (1-40) or human Agrin. Abeta (1-40) peptide sequence confirmed to correspond to human sequence following correspondence with author (GC). gcole@nccu.edu Mol. Cell. Neurosci. (1044-7431) 2000 Only protein-protein interactions imex curation Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Alzheimers - Interactions investigated in the context of Alzheimers disease cotman-2000-4 Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. human Homo sapiens Human light microscopy light microscopy immunostaining immunostaining Cotman SL., Halfter W., Cole GJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Paraffin or frozen sections of Alzheimer's disease brains pretreated with formic acid and stained woth polyclonal antisera recognising Abeta (1-40) or human Agrin. Abeta (1-40) peptide sequence confirmed to correspond to human sequence following correspondence with author (GC). gcole@nccu.edu Mol. Cell. Neurosci. (1044-7431) 2000 Only protein-protein interactions imex curation Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Alzheimers - Interactions investigated in the context of Alzheimers disease cotman-2000-5 Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. in vitro In vitro footprinting footprinting predetermined predetermined participant predetermined Cotman SL., Halfter W., Cole GJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Paraffin or frozen sections of Alzheimer's disease brains pretreated with formic acid and stained woth polyclonal antisera recognising Abeta (1-40) or human Agrin. Abeta (1-40) peptide sequence confirmed to correspond to human sequence following correspondence with author (GC). gcole@nccu.edu Mol. Cell. Neurosci. (1044-7431) 2000 Only protein-protein interactions imex curation Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Alzheimers - Interactions investigated in the context of Alzheimers disease cotman-2000-1 Agrin binds to beta-amyloid (Abeta), accelerates abeta fibril formation, and is localized to Abeta deposits in Alzheimer's disease brain. in vitro In vitro elisa enzyme linked immunosorbent assay ELISA ELISA elisa antibody detection identification by antibody antibody detection Cotman SL., Halfter W., Cole GJ. Apoptosis - Interactions involving proteins with a function related to apoptosis Paraffin or frozen sections of Alzheimer's disease brains pretreated with formic acid and stained woth polyclonal antisera recognising Abeta (1-40) or human Agrin. Abeta (1-40) peptide sequence confirmed to correspond to human sequence following correspondence with author (GC). gcole@nccu.edu Mol. Cell. Neurosci. (1044-7431) 2000 Only protein-protein interactions imex curation Neurodegeneration - Publications depicting interactions involved in neurodegenerative diseases. Alzheimers - Interactions investigated in the context of Alzheimers disease p05067-pro_0000000093 Amyloid-beta protein 40 APP A4 AD1 ABPP Alzheimer disease amyloid protein Cerebral vascular amyloid peptide PreA4 Protease nexin-II APPI Amyloid precursor protein Amyloid-beta A4 protein Alzheimer disease amyloid A4 protein homolog Amyloid-beta (A4) precursor protein protein protein human Homo sapiens Human DAEFRHDSGYEVHHQKLVFFAEDVGSNKGAIIGLMVGGVV 672 711 agrin_human Agrin AGRN AGRIN protein protein human Homo sapiens Human MAGRSHPGPLRPLLPLLVVAACVLPGAGGTCPERALERREEEANVVLTGTVEEILNVDPVQHTYSCKVRVWRYLKGKDLVARESLLDGGNKVVISGFGDPLICDNQVSTGDTRIFFVNPAPPYLWPAHKNELMLNSSLMRITLRNLEEVEFCVEDKPGTHFTPVPPTPPDACRGMLCGFGAVCEPNAEGPGRASCVCKKSPCPSVVAPVCGSDASTYSNECELQRAQCSQQRRIRLLSRGPCGSRDPCSNVTCSFGSTCARSADGLTASCLCPATCRGAPEGTVCGSDGADYPGECQLLRRACARQENVFKKFDGPCDPCQGALPDPSRSCRVNPRTRRPEMLLRPESCPARQAPVCGDDGVTYENDCVMGRSGAARGLLLQKVRSGQCQGRDQCPEPCRFNAVCLSRRGRPRCSCDRVTCDGAYRPVCAQDGRTYDSDCWRQQAECRQQRAIPSKHQGPCDQAPSPCLGVQCAFGATCAVKNGQAACECLQACSSLYDPVCGSDGVTYGSACELEATACTLGREIQVARKGPCDRCGQCRFGALCEAETGRCVCPSECVALAQPVCGSDGHTYPSECMLHVHACTHQISLHVASAGPCETCGDAVCAFGAVCSAGQCVCPRCEHPPPGPVCGSDGVTYGSACELREAACLQQTQIEEARAGPCEQAECGSGGSGSGEDGDCEQELCRQRGGIWDEDSEDGPCVCDFSCQSVPGSPVCGSDGVTYSTECELKKARCESQRGLYVAAQGACRGPTFAPLPPVAPLHCAQTPYGCCQDNITAARGVGLAGCPSACQCNPHGSYGGTCDPATGQCSCRPGVGGLRCDRCEPGFWNFRGIVTDGRSGCTPCSCDPQGAVRDDCEQMTGLCSCKPGVAGPKCGQCPDGRALGPAGCEADASAPATCAEMRCEFGARCVEESGSAHCVCPMLTCPEANATKVCGSDGVTYGNECQLKTIACRQGLQISIQSLGPCQEAVAPSTHPTSASVTVTTPGLLLSQALPAPPGALPLAPSSTAHSQTTPPPSSRPRTTASVPRTTVWPVLTVPPTAPSPAPSLVASAFGESGSTDGSSDEELSGDQEASGGGSGGLEPLEGSSVATPGPPVERASCYNSALGCCSDGKTPSLDAEGSNCPATKVFQGVLELEGVEGQELFYTPEMADPKSELFGETARSIESTLDDLFRNSDVKKDFRSVRLRDLGPGKSVRAIVDVHFDPTTAFRAPDVARALLRQIQVSRRRSLGVRRPLQEHVRFMDFDWFPAFITGATSGAIAAGATARATTASRLPSSAVTPRAPHPSHTSQPVAKTTAAPTTRRPPTTAPSRVPGRRPPAPQQPPKPCDSQPCFHGGTCQDWALGGGFTCSCPAGRGGAVCEKVLGAPVPAFEGRSFLAFPTLRAYHTLRLALEFRALEPQGLLLYNGNARGKDFLALALLDGRVQLRFDTGSGPAVLTSAVPVEPGQWHRLELSRHWRRGTLSVDGETPVLGESPSGTDGLNLDTDLFVGGVPEDQAAVALERTFVGAGLRGCIRLLDVNNQRLELGIGPGAATRGSGVGECGDHPCLPNPCHGGAPCQNLEAGRFHCQCPPGRVGPTCADEKSPCQPNPCHGAAPCRVLPEGGAQCECPLGREGTFCQTASGQDGSGPFLADFNGFSHLELRGLHTFARDLGEKMALEVVFLARGPSGLLLYNGQKTDGKGDFVSLALRDRRLEFRYDLGKGAAVIRSREPVTLGAWTRVSLERNGRKGALRVGDGPRVLGESPKSRKVPHTVLNLKEPLYVGGAPDFSKLARAAAVSSGFDGAIQLVSLGGRQLLTPEHVLRQVDVTSFAGHPCTRASGHPCLNGASCVPREAAYVCLCPGGFSGPHCEKGLVEKSAGDVDTLAFDGRTFVEYLNAVTESELANEIPVPETLDSGALHSEKALQSNHFELSLRTEATQGLVLWSGKATERADYVALAIVDGHLQLSYNLGSQPVVLRSTVPVNTNRWLRVVAHREQREGSLQVGNEAPVTGSSPLGATQLDTDGALWLGGLPELPVGPALPKAYGTGFVGCLRDVVVGRHPLHLLEDAVTKPELRPCPTP agrin_chick Agrin AGRN AGRIN protein protein chick Gallus gallus (Chicken) Chicken MGGSGAAATLALGLALGLALGGWANCPERELQRREEEANVVLTGTVEEIMNVDPVHHTYSCKVRVWRYLKGKDIVTHEILLDGGNKVVIGGFGDPLICDNQVSTGDTRIFFVNPAPQYMWPAHRNELMLNSSLMRITLRNLEEVEHCVEEHRKLLADKPNSYFTQTPPTPRDACRGMLCGFGAVCERSPTDPSQASCVCKKTACPVVVAPVCGSDYSTYSNECELEKAQCNQQRRIKVISKGPCGSKDPCAEVTCSFGSTCVRSADGQTAGCVCPASCSGVAESIVCGSDGKDYRSECDLNKHACDKQENVFKKFDGACDPCKGILNDMNRVCRVNPRTRRVELLSRPENCPSKREPVCGDDGVTYASECVMGRTGAIRGLEIQKVRSGQCQHQDKCKDECKFNAVCLKRWHARCSCDRITCDGTYRPVCARDSRTYSNDCERQKAECHQKAAIPVKHSGPCDLGTPSPCLSVECTFGATCVVKNREPVCECQQVCQGRYDPVCGSDNRTYGNPCELNAMACVLKREIRVKHKGPCDRCGKCQFGAICEAETGRCVCPTECVPSSQPVCGTDGNTYGSECELHVRACTQQKNILVAAQGDCKSCGTTVCSFGSTCVGGQCVCPRCEQQPLAQVCGTDGLTYDNRCELRAASCQQQKSIEVAKMGPCEDECGSGGSGSGDGSECEQDRCRHYGGWWDEDAEDDRCVCDFTCLAVPRSPVCGSDDVTYANECELKKTRCEKRQNLYVTSQGACRALTTTPPPLPVVHCSQTIYGCCPDNMTLALGVGAAGCPSTCQCNPYGSYGGTCDPATGQCSCKPGVGGLKCDRCEPGFWNFRGIVTDSKSGCTPCNCDPVGSVRDDCEQMTGLCSCKTGITGMKCNQCPNGSKMGMAGCEKDPSAPKSCEEMSCEFGATCVEVNGFAHCECPSPLCSEANMTKVCGSDGVTYGDQCQLKTIACRQGQLITVKHVGQCHESITHTSHTMPPTPLPTLPLDKLIVPPPLQLTTQAPEPTELATTSLLMEASPTTRSHPTTRRVTTTRPVTTPWMTHGVLKTTVRPLSTSPVVLATTQPPYAESGSAEGSGDQEMSISGDQESSGAGSAGEEEVEESQVTPTPAIERATCYNTPLGCCSDGKTAAADAEGSNCPATKVFQGVLILEEVEGQELFYTPEMADPKSELFGETARSIESALDELFRNSDVKNDFKSIRVRDLGQSSAVRVIVESHFDPATSYTAADVQAASLKQIRASKKRTILVKKPQQEHVKFMDFDWIPRIFTTTITTTTATTMAPATTRRHTTASAATTAHILRQDTVGHPSAKLAAPASTRRPTSTLPTTARRKPTRQPPSTTKKPSRPCDSHPCLHGGTCEDDGREFTCRCPAGKGGAVCEKPIRYFIPSFGGKSYLAFKMMKAYHTVRIAMEFRATELSGLLLYNGQNRGKDFISLALVGGFVELRFNTGSGTGVITSKVRVEPGKWHQLVVNRNRRSGMLAVDGEHVSGESPTGTDGLNLDTDLFVGGAPEDQMAVVAERTAATVGLKGSIRLLDVNNQMYDLREKGSDVLYGSGVGECGNDPCHPNPCHHGASCHVKEAEMFHCECLHSYTGPTCADERNPCDPTPCHISATCLVLPEGGAMCACPMGREGEFCERVTEQDHTMPFLPEFNGFSYLELNGLQTLFLTCRQMSMEVVFLAKSPSGMIFYNGQKTDGKGDFVSLALHDGYLEYRYDLGKGAAVLRSKEPVPLNTWISVLLERSGRKGVMRINNGERVMGESPKSRKVPHAFLNLKEPFYVGGAPDFSKLARAAAISTSFYGAVQRISIKGVPLLKEQHIRSAVEISTFRAHPCTQKPNPCQNGGTCSPRLESYECACQRGFSGAHCEKVIIEKAAGDAEAIAFDGRTYMEYHNAVTKSHLSNEIPAPDALDYPAEPSEKALQSNHFELSIKTEATQGLILWSGKGLERSDYIALAIVDGFVQMMYDLGSKPVVLRSTVPINTNHWTHIKAYRVQREGSLQVGNEAPITGSSPLGATQLDTDGALWLGGMERLSVAHKLPKAYSTGFIGCIRDVIVDRQELHLVEDALNNPTILHCSAK agrn-p05067pro-2 Agrin colocalises with beta amlyoid deposits in senile plaques in frontal cortex of Alzheimer's disease brain. 854058 n/a 854063 unspecified role unspecified role neutral component neutral component n/a 854064 unspecified role unspecified role neutral component neutral component colocalization colocalization false false false Immunostaing of Agrin and Abeta (1-40) observed in senile plaques in the frontal cortex of a 92 year old AD patient. Human Agrin antibody generated by rabbit immunization with a human agrin fusion protein (amino acids 780-1210) representing the N terminal half of the protein. anti Abeta (1-40) was purchased from Sigma. Fig 6A and B agrn-p05067pro-3 Agrin colocalises with beta amlyoid deposits in microvasculature of Alzheimer's disease brain. 854058 n/a 854063 unspecified role unspecified role neutral component neutral component n/a 854064 unspecified role unspecified role neutral component neutral component colocalization colocalization false false false Immunostaing of Agrin and Abeta (1-40) observed in the microvasculature in the frontal cortex of a 92 year old patient. Human Agrin antibody generated by rabbit immunization with a human agrin fusion protein (amino acids 780-1210) representing the N terminal half of the protein. anti Abeta (1-40) was purchased from Sigma. Fig 6E and F agrn-p05067pro Agrin coprecipitates with Abeta (1-40). 854059 n/a 854063 unspecified role unspecified role prey prey n/a 854065 unspecified role unspecified role bait bait chick Gallus gallus (Chicken) Chicken physical association physical association false false false Fig. 4 agrn-p05067pro Agrin colocalises with beta amlyoid deposits in neuritic plaques in hippocampus of Alzheimer's disease brain. 854060 n/a 854063 unspecified role unspecified role neutral component neutral component n/a 854064 unspecified role unspecified role neutral component neutral component colocalization colocalization false false false Immunostaing of Agrin and Abeta (1-40) observed in neuritic plaques in the hippocampus of a 62 year old AD patient. Human Agrin antibody generated by rabbit immunization with a human agrin fusion protein (amino acids 780-1210) representing the N terminal half of the protein. anti Abeta (1-40) was purchased from Sigma. Fig 6C and D agrn-p05067pro-1 Agrin binds to fibrillar, but not nonfibrillar Abeta (1-40). 854061 n/a 854065 unspecified role unspecified role neutral component neutral component chick Gallus gallus (Chicken) Chicken n/a 854063 unspecified role unspecified role neutral component neutral component direct interaction direct interaction false false false Fig. 2 agrn-p05067pro Agrin binds to fibrillar, but not nonfibrillar Abeta (1-40). 854062 n/a 854063 unspecified role unspecified role prey prey n/a 854065 unspecified role unspecified role bait bait chick Gallus gallus (Chicken) Chicken direct interaction direct interaction false false false Nitrous acid treatment (removal of heparan sulphate GAG side chains)of Agrin almost completly abolished binding to fibrilla Abeta. Non fibrilla Abeta did not bind to Agrin. Fig. 1